Traffic to the Malaria Parasite Food Vacuole: A NOVEL PATHWAY INVOLVING A PHOSPHATIDYLINOSITOL 3-PHOSPHATE-BINDING PROTEIN

McIntosh, M. T. and Vaid, A. and Hosgood, H. D. and Vijay, J. and Bhattacharya, A. and Sahani, M. H. and Baevova, P. and Joiner, K. A. and Sharma, P. (2007) Traffic to the Malaria Parasite Food Vacuole: A NOVEL PATHWAY INVOLVING A PHOSPHATIDYLINOSITOL 3-PHOSPHATE-BINDING PROTEIN. Journal of Biological Chemistry, 282 (15). pp. 11499-11508. ISSN 0021-9258

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Official URL: http://dx.doi.org/10.1074/jbc.M610974200

Abstract

Phosphatidylinositol 3-phosphate (PI3P) is a key ligand for recruitment of endosomal regulatory proteins in higher eukaryotes. Subsets of these endosomal proteins possess a highly selective PI3P binding zinc finger motif belonging to the FYVE domain family.We have identified a single FYVE domaincontaining protein in Plasmodium falciparum which we term FCP. Expression and mutagenesis studies demonstrate that key residues are involved in specific binding to PI3P. In contrast to FYVE proteins in other organisms, endogenous FCP localizes to a lysosomal compartment, the malaria parasite food vacuole (FV), rather than to cytoplasmic endocytic organelles. Transfections of deletion mutants further indicate that FCP is essential for trophozoite and FV maturation and that it traffics to the FV via a novel constitutive cytoplasmic to vacuole targeting pathway. This newly discovered pathway excludes the secretory pathway and is directed by a C-terminal 44-amino acid peptide domain. We conclude that an FYVE protein that might be expected to participate in vesicle targeting in the parasite cytosol instead has a vital and functional role in the malaria parasite FV.

Item Type: Article
Subjects: Pharmaceutical Sciences
Divisions: College of Pharmacy > Pharmacy
Depositing User: Dr Justin Louis
Date Deposited: 31 May 2017 10:56
Last Modified: 31 May 2017 10:56
URI: http://eprints.kku.edu.sa/id/eprint/766

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